HBE_HUMAN
ID HBE_HUMAN Reviewed; 147 AA.
AC P02100; Q6FH44;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Hemoglobin subunit epsilon;
DE AltName: Full=Epsilon-globin;
DE AltName: Full=Hemoglobin epsilon chain;
GN Name=HBE1; Synonyms=HBE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6254663; DOI=10.1016/0092-8674(80)90425-0;
RA Baralle F.E., Shoulders C.C., Proudfoot N.J.;
RT "The primary structure of the human epsilon-globin gene.";
RL Cell 21:621-626(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=6172865;
RA Clegg J.B.;
RT "Embryonic hemoglobin: sequence of the epsilon and zeta chains.";
RL Tex. Rep. Biol. Med. 40:23-28(1980).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-51, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF HB GOWER-2 IN COMPLEX WITH HEME,
RP AND SUBUNIT.
RX PubMed=9665850; DOI=10.1006/jmbi.1998.1868;
RA Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T., Baker E.N.;
RT "Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form
RT of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution.";
RL J. Mol. Biol. 280:475-484(1998).
CC -!- FUNCTION: The epsilon chain is a beta-type chain of early mammalian
CC embryonic hemoglobin.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two epsilon chains in
CC early embryonic hemoglobin Gower-2; two zeta chains and two epsilon
CC chains in early embryonic hemoglobin Gower-1.
CC {ECO:0000269|PubMed:9665850}.
CC -!- INTERACTION:
CC P02100; P69905: HBA2; NbExp=4; IntAct=EBI-6190240, EBI-714680;
CC P02100; P09105: HBQ1; NbExp=3; IntAct=EBI-6190240, EBI-10193656;
CC P02100; P02008: HBZ; NbExp=6; IntAct=EBI-6190240, EBI-719843;
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U01317; AAA16330.1; -; Genomic_DNA.
DR EMBL; V00508; CAA23766.1; -; Genomic_DNA.
DR EMBL; CR541912; CAG46710.1; -; mRNA.
DR EMBL; CH471064; EAW68802.1; -; Genomic_DNA.
DR EMBL; BC015537; AAH15537.1; -; mRNA.
DR CCDS; CCDS7756.1; -.
DR PIR; A90802; HEHU.
DR RefSeq; NP_005321.1; NM_005330.3.
DR PDB; 1A9W; X-ray; 2.90 A; E/F=2-147.
DR PDBsum; 1A9W; -.
DR AlphaFoldDB; P02100; -.
DR SMR; P02100; -.
DR BioGRID; 109296; 13.
DR ComplexPortal; CPX-2927; Hemoglobin E complex.
DR ComplexPortal; CPX-2928; Embryonic hemoglobin Gower-1 complex.
DR IntAct; P02100; 8.
DR STRING; 9606.ENSP00000369586; -.
DR iPTMnet; P02100; -.
DR PhosphoSitePlus; P02100; -.
DR BioMuta; HBE1; -.
DR DMDM; 122726; -.
DR jPOST; P02100; -.
DR MassIVE; P02100; -.
DR MaxQB; P02100; -.
DR PaxDb; P02100; -.
DR PeptideAtlas; P02100; -.
DR PRIDE; P02100; -.
DR ProteomicsDB; 51516; -.
DR Antibodypedia; 42207; 181 antibodies from 25 providers.
DR DNASU; 3046; -.
DR Ensembl; ENST00000292896.3; ENSP00000292896.2; ENSG00000213931.7.
DR Ensembl; ENST00000380237.5; ENSP00000369586.1; ENSG00000213931.7.
DR Ensembl; ENST00000396895.3; ENSP00000380104.2; ENSG00000213931.7.
DR GeneID; 3046; -.
DR KEGG; hsa:3046; -.
DR MANE-Select; ENST00000396895.3; ENSP00000380104.2; NM_005330.4; NP_005321.1.
DR UCSC; uc001mal.2; human.
DR CTD; 3046; -.
DR DisGeNET; 3046; -.
DR GeneCards; HBE1; -.
DR HGNC; HGNC:4830; HBE1.
DR HPA; ENSG00000213931; Low tissue specificity.
DR MIM; 142100; gene.
DR neXtProt; NX_P02100; -.
DR OpenTargets; ENSG00000213931; -.
DR PharmGKB; PA29205; -.
DR VEuPathDB; HostDB:ENSG00000213931; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000157809; -.
DR HOGENOM; CLU_003827_10_0_1; -.
DR InParanoid; P02100; -.
DR OMA; INGLWSK; -.
DR OrthoDB; 1370439at2759; -.
DR PhylomeDB; P02100; -.
DR TreeFam; TF333268; -.
DR PathwayCommons; P02100; -.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P02100; -.
DR SIGNOR; P02100; -.
DR BioGRID-ORCS; 3046; 13 hits in 1074 CRISPR screens.
DR ChiTaRS; HBE1; human.
DR EvolutionaryTrace; P02100; -.
DR GeneWiki; HBE1; -.
DR GenomeRNAi; 3046; -.
DR Pharos; P02100; Tbio.
DR PRO; PR:P02100; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P02100; protein.
DR Bgee; ENSG00000213931; Expressed in adrenal tissue and 89 other tissues.
DR ExpressionAtlas; P02100; baseline and differential.
DR Genevisible; P02100; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; IPI:ComplexPortal.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0031721; F:hemoglobin alpha binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0015671; P:oxygen transport; IDA:ComplexPortal.
DR GO; GO:0010942; P:positive regulation of cell death; IC:ComplexPortal.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR CDD; cd08925; Hb-beta-like; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR002337; Hemoglobin_b.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00814; BETAHAEM.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6172865"
FT CHAIN 2..147
FT /note="Hemoglobin subunit epsilon"
FT /id="PRO_0000053212"
FT BINDING 64
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000250|UniProtKB:P80044"
FT BINDING 93
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000269|PubMed:9665850,
FT ECO:0007744|PDB:1A9W"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 143
FT /note="A -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:1A9W"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1A9W"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:1A9W"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:1A9W"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1A9W"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:1A9W"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:1A9W"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1A9W"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:1A9W"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:1A9W"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1A9W"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:1A9W"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1A9W"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:1A9W"
SQ SEQUENCE 147 AA; 16203 MW; 223388816EDDE8D5 CRC64;
MVHFTAEEKA AVTSLWSKMN VEEAGGEALG RLLVVYPWTQ RFFDSFGNLS SPSAILGNPK
VKAHGKKVLT SFGDAIKNMD NLKPAFAKLS ELHCDKLHVD PENFKLLGNV MVIILATHFG
KEFTPEVQAA WQKLVSAVAI ALAHKYH